3IN1
Crystal structure of a putative Ribokinase in complex with ADP from E.coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0006974 | biological_process | DNA damage response |
| A | 0008673 | molecular_function | 2-dehydro-3-deoxygluconokinase activity |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| A | 0019200 | molecular_function | carbohydrate kinase activity |
| A | 0019698 | biological_process | D-galacturonate catabolic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042840 | biological_process | D-glucuronate catabolic process |
| A | 0046835 | biological_process | carbohydrate phosphorylation |
| B | 0005829 | cellular_component | cytosol |
| B | 0006974 | biological_process | DNA damage response |
| B | 0008673 | molecular_function | 2-dehydro-3-deoxygluconokinase activity |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| B | 0019200 | molecular_function | carbohydrate kinase activity |
| B | 0019698 | biological_process | D-galacturonate catabolic process |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0042840 | biological_process | D-glucuronate catabolic process |
| B | 0046835 | biological_process | carbohydrate phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP A 510 |
| Chain | Residue |
| A | ASN196 |
| A | HOH394 |
| A | NA411 |
| A | HOH414 |
| A | HOH417 |
| A | LYS227 |
| A | GLY229 |
| A | LYS230 |
| A | GLY232 |
| A | ALA246 |
| A | THR255 |
| A | ASN284 |
| A | ALA287 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 411 |
| Chain | Residue |
| A | THR255 |
| A | ALA258 |
| A | GLY259 |
| A | ADP510 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP B 510 |
| Chain | Residue |
| B | ASN196 |
| B | LYS227 |
| B | GLY229 |
| B | GLY232 |
| B | ALA246 |
| B | VAL247 |
| B | ILE250 |
| B | ALA252 |
| B | THR255 |
| B | ASN284 |
| B | ALA287 |
| B | HOH385 |
| B | NA411 |
| B | HOH421 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA B 411 |
| Chain | Residue |
| B | GLY259 |
| B | ADP510 |
Functional Information from PROSITE/UniProt
| site_id | PS00583 |
| Number of Residues | 25 |
| Details | PFKB_KINASES_1 pfkB family of carbohydrate kinases signature 1. GGdAiNEAtiIsRLGhrtalmsriG |
| Chain | Residue | Details |
| A | GLY41-GLY65 |
| site_id | PS00584 |
| Number of Residues | 14 |
| Details | PFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTiGAGDnfaSGFI |
| Chain | Residue | Details |
| A | ASP254-ILE267 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| A | ASP260 | |
| A | ARG108 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| B | ASP260 | |
| B | ARG108 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| A | GLY259 | |
| A | GLY257 | |
| A | ALA258 | |
| A | ASP260 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| B | GLY259 | |
| B | GLY257 | |
| B | ALA258 | |
| B | ASP260 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| A | GLY257 | |
| A | LYS227 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| B | GLY257 | |
| B | LYS227 |
